ID G3H290_CRIGR Unreviewed; 1069 AA.
AC G3H290;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Acyl-CoA dehydrogenase family member 10 {ECO:0000313|EMBL:EGW07432.1, ECO:0000313|Ensembl:ENSCGRP00001020131.1};
GN Name=Acad10 {ECO:0000313|Ensembl:ENSCGRP00001020131.1,
GN ECO:0000313|RefSeq:XP_027269882.1};
GN ORFNames=I79_004261 {ECO:0000313|EMBL:EGW07432.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07432.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGW07432.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCGRP00001020131.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:XP_027269882.1}
RP IDENTIFICATION.
RC STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027269882.1};
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_027269882.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; JH000113; EGW07432.1; -; Genomic_DNA.
DR RefSeq; XP_003498473.1; XM_003498425.3.
DR RefSeq; XP_027269882.1; XM_027414081.2.
DR STRING; 10029.G3H290; -.
DR PaxDb; 10029-XP_007628875-1; -.
DR Ensembl; ENSCGRT00001024375.1; ENSCGRP00001020131.1; ENSCGRG00001019367.1.
DR GeneID; 100763570; -.
DR KEGG; cge:100763570; -.
DR CTD; 80724; -.
DR eggNOG; KOG1469; Eukaryota.
DR eggNOG; KOG3085; Eukaryota.
DR GeneTree; ENSGT00940000161620; -.
DR OMA; KNWNFYM; -.
DR OrthoDB; 276350at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000694386; Unplaced.
DR Proteomes; UP001108280; Chromosome 4.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR CDD; cd02603; HAD_sEH-N_like; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR02247; HAD-1A3-hyp; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR47829:SF1; AMINOGLYCOSIDE PHOSPHOTRANSFERASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47829; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12880)-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT DOMAIN 288..509
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT DOMAIN 666..786
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 791..892
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 904..1052
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 1069 AA; 119396 MW; 527ABA0CE2115727 CRC64;
MSIRKLFQMS ALQWAWRTAA MKSTPGRQQG ALRWTRSGGH SYRAVIFDMG GVLMPSPGTV
AAEWEVQNRI PSGTIMKAFV RDGDSGPWMR FLRGERTTEG FLEEFGKLCS EIAKTSVPVN
SFFSLITSEQ LTKQFPVMTQ AISQIRARGL QTAILTNNFY LSNGKSFLPL DRKQFDVVVE
SCLEGISKPD PRIYQLCLQR LGLQPSEAIF LDDLGSNLKA AASLGIHTIK VDHPETAVKE
LEALLGFPLC VGVPNTGPVR KTMEIAEDAL EKYLKGLLGT HDTGPMELLQ FDHGQSNPTY
YIRLADRQLV LRKKPPGTLL PSAHAIEREF RIMKALRNAG VPVPTVLDLC EDSSIIGTPF
YLMEYCPGII YKDPSLPGLE PSRRRAIYTA MSQVLCRIHS VDLQATGLDS FGKQGDYIPR
QVQTWTKQYR AAETSSIPAM ERLIQWLPLH LPRQQRTTVV HGDFRLDNLI FHPEKSEVLA
VLDWELSTLG DPFADVAYSC LAHYLPSDFP MLRGFRDQDV TQLGIPTVEE YFRTYCLHMG
IPPVDNWNFY MAFSFFRVAA ILQGVYKRSL TGQASSATAK QSGKLTEFMA ELAWDFAIKE
GFRVFKEMPA TKPQVRSYHA WAGLRPQWTL AGLRSYSTVA AASPPQETKG GLIISPEGLS
PRVRKLYDRL LQFMEQNVYP LEPELQRHQA SADRWSPSPL IEDLKEKAKA EGLWNLFLPL
ETDPEKKYGA GLTNMEYAHL CEVMGMSLYA SEVFNCSAPD TGNMELLVRY GTEEQKARWL
VPLLEGRIRS CFAMTEPQVA SSDASNIEAS IKEEDGSYVI NGHKWWISGI LDPRCKLCVF
MGKTDPQAPR HQQQSMVLVP MDTPGISVIR PLSVYGLEDA PGGHGEVWFK DVRVPKENIV
LGPGRGFEIA QGRLGPGRIH HCMRLIGFSE RALALMKTRV MSRTAFGKPL VEHGTILADI
ARSRVDIEQA RLLVLKAAHL MDVTGNKAAA LEIAMIKMVA PSMAYQVIDR AIQAFGAAGL
GSDYPLAQFF AWARALRFAD GPDEVHRLTV AKMELKNPSR LQEPAVPRV
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